SNaPe: a versatile method to generate multiplexed protein fusions using synthetic linker peptides forin vitroapplications

2016 ◽  
Vol 23 (1) ◽  
pp. 16-27 ◽  
Author(s):  
Veronika Ulrich ◽  
Max J. Cryle
Keyword(s):  
Linker Peptides

scholarly journals Stable linker peptides for a cellulose-binding domain–lipase fusion protein expressed in Pichia pastoris

2001 ◽  
Vol 14 (9) ◽  
pp. 711-715 ◽  
Author(s):  
Malin Gustavsson ◽  
Janne Lehtiö ◽  
Stuart Denman ◽  
Tuula T. Teeri ◽  
Karl Hult ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Fusion Protein ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Linker Peptides ◽  
Cellulose Binding

Interactions Between Family 3 Carbohydrate Binding Modules (CBMs) and Cellulosomal Linker Peptides

2012 ◽  
pp. 247-259 ◽  
Author(s):  
Oren Yaniv ◽  
Felix Frolow ◽  
Maly Levy-Assraf ◽  
Raphael Lamed ◽  
Edward A. Bayer
Keyword(s):  
Carbohydrate Binding ◽  
Carbohydrate Binding Modules ◽  
Linker Peptides

scholarly journals Global mitotic phosphorylation of C2H2zinc finger protein linker peptides

Cell Cycle ◽  
2011 ◽  
Vol 10 (19) ◽  
pp. 3327-3336 ◽  
Author(s):  
Raed Rizkallah ◽  
Karen E. Alexander ◽  
Myra M. Hurt
Keyword(s):  
Finger Protein ◽  
Linker Peptides ◽  
Mitotic Phosphorylation

Design and assembly of anti-CD16 ScFv antibody with two different linker peptides

2003 ◽  
Vol 282 (1-2) ◽  
pp. 33-43 ◽  
Author(s):  
Jiannan Feng ◽  
Zhigang Xie ◽  
Ning Guo ◽  
Beifen Shen
Keyword(s):  
Scfv Antibody ◽  
Linker Peptides

Activation of Calpain by Ca2+: Roles of the Large Subunit N-terminal and Domain III–IV Linker Peptides

2004 ◽  
Vol 343 (4) ◽  
pp. 1049-1053 ◽  
Author(s):  
Christopher M. Hosfield ◽  
John S. Elce ◽  
Zongchao Jia
Keyword(s):  
Large Subunit ◽  
Linker Peptides ◽  
Domain Iii

scholarly journals The Coevolution of Phycobilisomes: Molecular Structure Adapting to Functional Evolution

2011 ◽  
Vol 2011 ◽  
pp. 1-9 ◽  
Author(s):  
Fei Shi ◽  
Song Qin ◽  
Yin-Chu Wang
Keyword(s):  
Red Alga ◽  
Adaptive Selection ◽  
Light Harvesting Complex ◽  
Physical Chemical ◽  
Coevolution Analysis ◽  
Selective Evolution ◽  
Linker Peptides ◽  
The Stability ◽  
Unidirectional Transfer ◽  
Covariation Analysis

Phycobilisome is the major light-harvesting complex in cyanobacteria and red alga. It consists of phycobiliproteins and their associated linker peptides which play key role in absorption and unidirectional transfer of light energy and the stability of the whole complex system, respectively. Former researches on the evolution among PBPs and linker peptides had mainly focused on the phylogenetic analysis and selective evolution. Coevolution is the change that the conformation of one residue is interrupted by mutation and a compensatory change selected for in its interacting partner. Here, coevolutionary analysis of allophycocyanin, phycocyanin, and phycoerythrin and covariation analysis of linker peptides were performed. Coevolution analyses reveal that these sites are significantly correlated, showing strong evidence of the functional and structural importance of interactions among these residues. According to interprotein coevolution analysis, less interaction was found between PBPs and linker peptides. Our results also revealed the correlations between the coevolution and adaptive selection in PBS were not directly related, but probably demonstrated by the sites coupled under physical-chemical interactions.

Functional Characterization of Permuted Enhanced Green Fluorescent Proteins Comprising Varying Linker Peptides¶

2007 ◽  
Vol 74 (2) ◽  
pp. 356-363 ◽  
Author(s):  
Walther Akemann ◽  
Christopher Dinesh Raj ◽  
Thomas Knöpfel
Keyword(s):  
Fluorescent Proteins ◽  
Functional Characterization ◽  
Green Fluorescent Proteins ◽  
Linker Peptides ◽  
Green Fluorescent

Enhancement of engineered trifunctional enzyme by optimizing linker peptides for degradation of agricultural by-products

2010 ◽  
Vol 47 (5) ◽  
pp. 194-199 ◽  
Author(s):  
Ruili Wang ◽  
Yemin Xue ◽  
Xixi Wu ◽  
Xiangfei Song ◽  
Jingjing Peng
Keyword(s):  
Linker Peptides ◽  
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